Document Detail


Engineering of 2-Cys peroxiredoxin for enhanced stress-tolerance.
MedLine Citation:
PMID:  21773675     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A typical 2-cysteine peroxiredoxin (2-Cys Prx)-like protein (PpPrx) that alternatively acts as a peroxidase or a molecular chaperone in Pseudomonas putida KT2440 was previously characterized. The dual functions of PpPrx are regulated by the existence of an additional Cys(112) between the active Cys(51) and Cys(171) residues. In the present study, additional Cys residues (Cys(31), Cys(112), and Cys(192)) were added to PpPrx variants to improve their enzymatic function. The optimal position of the additional Cys residues for the dual functionality was assessed. The peroxidase activities of the S31C and Y192C mutants were increased 3- to 4-fold compared to the wild-type, while the chaperone activity was maintained at > 66% of PpPrx. To investigate whether optimization of the dual functions could enhance stress-tolerance in vivo, a complementation study was performed. The S31C and Y192C mutants showed a much greater tolerance than other variants under a complex condition of heat and oxidative stresses. The optimized dual functions of PpPrx could be adapted for use in bioengineering systems and industries, such as to develop organisms that are more resistant to extreme environments.
Authors:
Byung Chull An; Seung Sik Lee; Jae Taek Lee; Sung Hyun Hong; Seung Gon Wi; Byung Yeoup Chung
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-07-15
Journal Detail:
Title:  Molecules and cells     Volume:  32     ISSN:  0219-1032     ISO Abbreviation:  Mol. Cells     Publication Date:  2011 Sep 
Date Detail:
Created Date:  2011-09-30     Completed Date:  2012-01-30     Revised Date:  2014-02-23    
Medline Journal Info:
Nlm Unique ID:  9610936     Medline TA:  Mol Cells     Country:  United States    
Other Details:
Languages:  eng     Pagination:  257-64     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  metabolism*
Cloning, Molecular
Cysteine / chemistry,  genetics,  metabolism*
Escherichia coli / drug effects*,  genetics,  metabolism
Hot Temperature
Hydrogen Peroxide / pharmacology
Kinetics
Molecular Chaperones / chemistry,  genetics,  metabolism*
Molecular Sequence Data
Mutagenesis, Site-Directed
Oxidative Stress
Peroxiredoxins / chemistry,  genetics,  metabolism*
Plasmids
Protein Engineering / methods*
Pseudomonas putida / chemistry,  enzymology*
Recombinant Proteins / chemistry,  genetics,  metabolism*
Stress, Physiological
Transformation, Bacterial
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Molecular Chaperones; 0/Recombinant Proteins; BBX060AN9V/Hydrogen Peroxide; EC 1.11.1.15/Peroxiredoxins; K848JZ4886/Cysteine
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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